SARS Envelope, His
Protein is >90% pure as determined SDS-PAGE.
Description
The E.coli derived recombinant protein contains the Envelope protein 1-76 amino acids immunodominant regions fused to 6xHis tag at C-terminal.
Product Specs
The SARS Associated Coronavirus Envelope protein is a small membrane protein that plays a crucial role in the virus's life cycle. It is essential for viral assembly, budding, envelope formation, and pathogenesis. The virus possesses three outer structural proteins: membrane (M), envelope (E), and spike (S) proteins. The spike (S) glycoprotein interacts with a cellular receptor, mediating membrane fusion for viral entry into target cells. Therefore, the S-protein is critical in the virus infection cycle and is the primary target of neutralizing antibodies.
This recombinant protein is derived from E. coli and consists of the Envelope protein's immunodominant region, spanning amino acids 1-76, fused to a C-terminal 6xHis tag.
The SARS Envelope protein solution is supplied in phosphate-buffered saline (PBS).
The protein is shipped with ice packs. Upon receipt, store it at -20°C.
SDS-PAGE analysis indicates that the protein purity is greater than 90%.
Purified by proprietary chromatographic technique.
Immunoreactive with sera of SARS-infected individuals.
Product Science Overview
The SARS-associated coronavirus (SARS-CoV) is a member of the Coronaviridae family, known for causing severe acute respiratory syndrome (SARS). The envelope (E) protein of SARS-CoV is a small, integral membrane protein that plays a crucial role in the virus’s life cycle, including assembly, budding, envelope formation, and pathogenesis .
The E protein is a multifunctional protein involved in several aspects of the viral life cycle. It is a small protein, typically around 76-109 amino acids in length, and is characterized by its hydrophobic transmembrane domain. This domain allows the E protein to embed itself into the lipid bilayer of the host cell membrane .
The E protein functions as an ion channel, also known as a viroporin, which is essential for the virus’s ability to alter the host cell environment to favor viral replication. It interacts with other viral proteins, such as the membrane (M) protein, to facilitate the assembly and release of new virions .
Recombinant proteins are artificially produced proteins that are generated through recombinant DNA technology. The His tag, or polyhistidine tag, is a sequence of histidine residues added to the protein to facilitate purification and detection. The His tag binds to metal ions, allowing the recombinant protein to be easily isolated using metal affinity chromatography .
The recombinant SARS-CoV E protein with a His tag is used in various research applications, including structural studies, vaccine development, and the study of protein-protein interactions. The His tag allows researchers to purify the E protein efficiently and study its properties in detail .
The E protein is a target for vaccine development due to its critical role in the viral life cycle. DNA vaccines expressing the E protein have been shown to elicit cellular immune responses, making them potential candidates for cross-protective vaccines against different coronaviruses .
In addition to vaccine development, the recombinant E protein is used in structural studies to understand its role in the virus’s life cycle. By studying the E protein’s structure and interactions with other viral and host proteins, researchers can identify potential targets for antiviral drugs .
